EC Number | Cloned (Comment) | Organism |
---|---|---|
2.7.7.43 | a series of deletions from the 3'-end of the CMP-NeuAc synthetase coding region is constructed and expressed in Escherichia coli | Escherichia coli |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.7.7.43 | DELTA1-227 | mutant enzyme shows no CMP-N-acetylneuraminic acid synthetase activity, mutant enzyme is able to hydrolyze platelet activating factor | Escherichia coli |
2.7.7.43 | DELTA1-229 | mutant enzyme shows no CMP-N-acetylneuraminic acid synthetase activity, mutant enzyme is not able to hydrolyze platelet activating factor | Escherichia coli |
2.7.7.43 | DELTA230-418 | mutant enzyme shows 43% of the wild-type activity with CTP and N-acylneuraminate as substrates, decrease in stability compared to wild-type enzyme | Escherichia coli |
2.7.7.43 | DELTA247-418 | mutant enzyme shows 15% of the wild-type activity with CTP and N-acylneuraminate as substrates, decrease in stability compared to wild-type enzyme | Escherichia coli |
2.7.7.43 | DELTA340-418 | mutant enzyme shows 65% of the wild-type activity with CTP and N-acylneuraminate as substrates, as stable as wild-type enzyme | Escherichia coli |
2.7.7.43 | DELTA384-418 | mutant enzyme shows 31% of the wild-type activity with CTP and N-acylneuraminate as substrates, as stable as wild-type enzyme | Escherichia coli |
2.7.7.43 | DELTA396-418 | mutant enzyme shows 38% of the wild-type activity with CTP and N-acylneuraminate as substrates, as stable as wild-type enzyme | Escherichia coli |
2.7.7.43 | additional information | a series of deletions from the 3'-end of the CMP-NeuAc synthetase coding region is constructed and expressed in Escherichia coli. As a result, the catalytic domain required for CMP-NeuAc synthetase is found to be in the N-terminal half consisting of amino acids 1229. The C-terminal half consisting of amino acids 228418 exhibits platelet-activating factor acetylhydrolase activity | Escherichia coli |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.7.43 | CTP + N-acylneuraminate | Escherichia coli | CMP-NeuAc is essential for the formation of capsule polysialylate for strain K1 | diphosphate + CMP-N-acylneuraminate | - |
? | |
2.7.7.43 | CTP + N-acylneuraminate | Escherichia coli K1 | CMP-NeuAc is essential for the formation of capsule polysialylate for strain K1 | diphosphate + CMP-N-acylneuraminate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.7.43 | Escherichia coli | - |
- |
- |
2.7.7.43 | Escherichia coli K1 | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.7.7.43 | wild-type enzyme and mutant enzymes | Escherichia coli |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.7.7.43 | 0.0017 | - |
mutant enzyme DELTA1-227 | Escherichia coli |
2.7.7.43 | 0.0113 | - |
wild-type enzyme | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.7.43 | CTP + N-acylneuraminate | - |
Escherichia coli | diphosphate + CMP-N-acylneuraminate | - |
? | |
2.7.7.43 | CTP + N-acylneuraminate | CMP-NeuAc is essential for the formation of capsule polysialylate for strain K1 | Escherichia coli | diphosphate + CMP-N-acylneuraminate | - |
? | |
2.7.7.43 | CTP + N-acylneuraminate | - |
Escherichia coli K1 | diphosphate + CMP-N-acylneuraminate | - |
? | |
2.7.7.43 | CTP + N-acylneuraminate | CMP-NeuAc is essential for the formation of capsule polysialylate for strain K1 | Escherichia coli K1 | diphosphate + CMP-N-acylneuraminate | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.7.7.43 | CMP-N-acetylneuraminic acid synthetase | - |
Escherichia coli |
2.7.7.43 | CMP-NeuAc synthetase | - |
Escherichia coli |